Your browser does not support inline frames or is currently configured not to display inline frames. Content can be viewed at actual source page: inc/head.html
Go to PDB code:
Transferase
PDB id
3ci6
Contents
Protein chains
158 a.a.
*
166 a.a.
*
Ligands
P4G
×2
PEG
×2
GOL
×2
Waters
×285
*
Residue conservation analysis
PDB id:
3ci6
Links
PDBe
RCSB
SRS
MMDB
JenaLib
OCA
PDBWiki
Proteopedia
CATH
SCOP
FSSP
HSSP
PDBSWS
PQS
ProSAT
EDS
Whatcheck
Name:
Transferase
Title:
Crystal structure of the gaf domain from acinetobacter phosphoenolpyruvate-protein phosphotransferase
Structure:
Phosphoenolpyruvate-protein phosphotransferase. Chain: a, b. Fragment: gaf domain: residues 1-168. Engineered: yes
Source:
Acinetobacter sp.. Organism_taxid: 62977. Strain: adp1. Gene: ptsp, aciad0454. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
1.55Å
R-factor:
0.170
R-free:
0.196
Authors:
M.E.Cuff,G.Shackelford,Y.Kim,A.Joachimiak,Midwest Center For Structural Genomics (Mcsg)
Key ref:
M.E.Cuff et al. Crystal structure of the gaf domain from acinetobacter phosphoenolpyruvate-Protein phosphotransferase..
To be published
,
Date:
10-Mar-08
Release date:
13-May-08
PROCHECK
Headers
References
Protein chain
?
Q6FEW8
(Q6FEW8_ACIAD) - Phosphoenolpyruvate-protein phosphotransferase
Seq:
Struc:
 
Seq:
Struc:
764 a.a.
158 a.a.
Protein chain
?
Q6FEW8
(Q6FEW8_ACIAD) - Phosphoenolpyruvate-protein phosphotransferase
Seq:
Struc:
 
Seq:
Struc:
764 a.a.
166 a.a.
Key:
PfamA domain
Secondary structure
CATH domain
Enzyme reactions
Enzyme class:
Chains A, B:
E.C.2.7.3.9
- Phosphoenolpyruvate--protein phosphotransferase.
[IntEnz]
[ExPASy]
[KEGG]
[BRENDA]
Reaction:
Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)- phospho-L-histidine
Phosphoenolpyruvate
+
protein L-histidine
=
pyruvate
Bound ligand (Het Group name =
GOL
)
matches with 71.43% similarity
+
protein N(pi)- phospho-L-histidine
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
Gene Ontology (GO) functional annotation
Biochemical function
protein binding
1 term